ID L0A9N7_CALLD Unreviewed; 460 AA.
AC L0A9N7;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE SubName: Full=Phosphomethylpyrimidine kinase {ECO:0000313|EMBL:AFZ70598.1};
GN OrderedLocusNames=Calag_0858 {ECO:0000313|EMBL:AFZ70598.1};
OS Caldisphaera lagunensis (strain DSM 15908 / JCM 11604 / ANMR 0165 /
OS IC-154).
OC Archaea; Thermoproteota; Thermoprotei; Acidilobales; Caldisphaeraceae;
OC Caldisphaera.
OX NCBI_TaxID=1056495 {ECO:0000313|EMBL:AFZ70598.1, ECO:0000313|Proteomes:UP000010469};
RN [1] {ECO:0000313|Proteomes:UP000010469}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15908 / JCM 11604 / IC-154
RC {ECO:0000313|Proteomes:UP000010469};
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Peters L., Mikhailova N., Teshima H.,
RA Kyrpides N., Mavromatis K., Ivanova N., Brettin T., Detter J.C., Han C.,
RA Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P.,
RA Woyke T., Wu D., Spring S., Schroeder M., Brambilla E., Klenk H.-P.,
RA Eisen J.A.;
RT "Complete genome of Caldisphaera lagunensis DSM 15908.";
RL Submitted (MAR-2012) to the EMBL/GenBank/DDBJ databases.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP003378; AFZ70598.1; -; Genomic_DNA.
DR RefSeq; WP_015232495.1; NC_019791.1.
DR AlphaFoldDB; L0A9N7; -.
DR STRING; 1056495.Calag_0858; -.
DR GeneID; 14212118; -.
DR KEGG; clg:Calag_0858; -.
DR eggNOG; arCOG00020; Archaea.
DR HOGENOM; CLU_035788_0_0_2; -.
DR InParanoid; L0A9N7; -.
DR OrthoDB; 43786at2157; -.
DR Proteomes; UP000010469; Chromosome.
DR GO; GO:0008972; F:phosphomethylpyrimidine kinase activity; IEA:InterPro.
DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro.
DR CDD; cd01169; HMPP_kinase; 1.
DR Gene3D; 3.40.1190.20; -; 1.
DR Gene3D; 3.40.225.10; Class II aldolase/adducin N-terminal domain; 1.
DR InterPro; IPR036409; Aldolase_II/adducin_N_sf.
DR InterPro; IPR004399; HMP/HMP-P_kinase_dom.
DR InterPro; IPR013749; PM/HMP-P_kinase-1.
DR InterPro; IPR029056; Ribokinase-like.
DR InterPro; IPR019293; ThiN.
DR NCBIfam; TIGR00097; HMP-P_kinase; 1.
DR PANTHER; PTHR20858:SF17; HYDROXYMETHYLPYRIMIDINE_PHOSPHOMETHYLPYRIMIDINE KINASE THI20-RELATED; 1.
DR PANTHER; PTHR20858; PHOSPHOMETHYLPYRIMIDINE KINASE; 1.
DR Pfam; PF08543; Phos_pyr_kin; 1.
DR Pfam; PF10120; ThiP_synth; 1.
DR SUPFAM; SSF53639; AraD/HMP-PK domain-like; 1.
DR SUPFAM; SSF53613; Ribokinase-like; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:AFZ70598.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000010469};
KW Transferase {ECO:0000313|EMBL:AFZ70598.1}.
FT DOMAIN 17..261
FT /note="Pyridoxamine kinase/Phosphomethylpyrimidine kinase"
FT /evidence="ECO:0000259|Pfam:PF08543"
SQ SEQUENCE 460 AA; 50772 MW; 5F2DD41F4E0EF315 CRC64;
MNKYKQIPVA LTIAGSDSGG GAGIAADLKT FASLGVHGTV AITSVTAQNT YEVTGIYDVT
PDMVRKQIEA VYNDFGIDAA KTGMLSNALI VEEVANTLKS YDFPLVIDPV MVSKSCAPLL
REDAVNILIK KLIPRATVIT PNIPEAEKIT NMKILNLDDA RKAAKIIVEE FGAKAAIVKG
GHMKGEESID VLYYNGEFRE FVGKRINTKS DHGTGCSFSA SITANLAKGY GIVESIKIAK
ELISNAIFYG LPLGKGHGPV NPISYMEIPY HKYMVYIEMK NALKLLDEKQ ELIAKLIPEI
STNLAMALPR FYARSIDDVI AVPGRIRKFK DKLIFAKEPE FGASDHVARA LLKFMDYFPE
YRSAANIAYN DDIKRIIEKL NFSYSYYDRK YEPKDVKEKE GGSMQWGIEF AIKNMSIKNM
SNPLDIIIDY GDFGKEPGAI IFGKTANEVV GKMIKIAELL
//